ID A9MQJ5_SALAR Unreviewed; 395 AA.
AC A9MQJ5;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Cystathionine beta-lyase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=SARI_04464 {ECO:0000313|EMBL:ABX24239.1};
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX24239.1, ECO:0000313|Proteomes:UP000002084};
RN [1] {ECO:0000313|EMBL:ABX24239.1, ECO:0000313|Proteomes:UP000002084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC {ECO:0000313|Proteomes:UP000002084};
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate;
CC Xref=Rhea:RHEA:13965, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58161, ChEBI:CHEBI:58199;
CC Evidence={ECO:0000256|ARBA:ARBA00001535};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362118};
CC -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
CC {ECO:0000256|ARBA:ARBA00009077, ECO:0000256|RuleBase:RU362118}.
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DR EMBL; CP000880; ABX24239.1; -; Genomic_DNA.
DR AlphaFoldDB; A9MQJ5; -.
DR STRING; 41514.SARI_04464; -.
DR KEGG; ses:SARI_04464; -.
DR HOGENOM; CLU_018986_5_1_6; -.
DR Proteomes; UP000002084; Chromosome.
DR GO; GO:0004121; F:cystathionine beta-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019346; P:transsulfuration; IEA:InterPro.
DR CDD; cd00614; CGS_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR InterPro; IPR006233; Cys_b_lyase_bac.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01324; cysta_beta_ly_B; 1.
DR PANTHER; PTHR43500; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR PANTHER; PTHR43500:SF1; CYSTATHIONINE BETA-LYASE-RELATED; 1.
DR Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR PIRSF; PIRSF001434; CGS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR001434-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002084}.
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001434-2"
SQ SEQUENCE 395 AA; 42897 MW; 59750531273CF723 CRC64;
MTNKQLDTKL VNAGRSKKYT LGSVNSVIQR ASSLVFDTIE AKKHATRNRA NGELFYGRRG
TLTHFSLQEA MCELEGGAGC ALFPCGAAAI ANTILAFVEQ GDHVLMTNTA YEPSQNFCSK
ILGKLGVTTS WFDPLIGADI IQHIQPNTKV VFLESPGSIT MEVHDIPTIV SAVRRVAPKA
VIMIDNTWAA GILFKALEFG IDISIQAGTK YLIGHSDAMV GTAVANARCW EQLRESAYLM
GQMLDADTAY MTSRGLRTLG VRLRQHHESS LKIAAWLTNH PQVARVNHPA LPGSQGHAIW
KRDFTGSSGL FSFVLNKKLT DAELSAYLDN FSLFSMAYSW GGFESLILAN QPEQIAAIRP
AGGVDFTGTL IRVHIGLENV DDLIADLAAG FARIV
//
